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Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody

nAChR α7, Cholinergic receptor nicotinic alpha 7, Neuronal acetylcholine receptor subunit alpha-7, ACRA7
Cat #: ANC-007
Alternative Name nAChR α7, Cholinergic receptor nicotinic alpha 7, Neuronal acetylcholine receptor subunit alpha-7, ACRA7
  • KO Validated
  • Lyophilized Powder yes
    Type: Polyclonal
    Host: Rabbit
    Reactivity: h, m, r
    Immunogen
    • Peptide (C)KELVKNYNPLER, corresponding to amino acid residues 31-42 of rat nAChRα7 (Accession Q05941). Extracellular, N-terminus.
    Accession (Uniprot) Number Q05941
    Gene ID 25302
    Peptide confirmation Confirmed by amino acid analysis and mass spectrometry.
    Homology Mouse, human - identical.
    RRID AB_10659339.
    Purity Affinity purified on immobilized antigen.
    Form Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.
    Isotype Rabbit IgG.
    Storage before reconstitution The antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C.
    Reconstitution 25 μl, 50 μl or 0.2 ml double distilled water (DDW), depending on the sample size.
    Antibody concentration after reconstitution 0.8 mg/ml.
    Storage after reconstitution The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing. Centrifuge all antibody preparations before use (10000 x g 5 min).
    Standard quality control of each lot Western blot analysis.
    Applications: ic, if, ifc, ih, lci, wb
    May also work in: ip*
    Western blot
    • Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain cell lysates:
      Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain cell lysates:
      1,2. Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody (#ANC-007), (1:200).
      3,4. Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody, preincubated with Nicotinic Acetylcholine Receptor α7/CHRNA7 (extracellular) Blocking Peptide (#BLP-NC007).
    Immunohistochemistry
    • Expression of nAChRα7 in rat DRG
      Expression of nAChRα7 in rat DRG
      Immunohistochemical staining of rat dorsal root ganglion (DRG) frozen sections using Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody (#ANC-007), (1:200). nAChRα7 (red staining) is expressed in DRG neurons. Hoechst 33342 is used as the counterstain (blue).
    Immunocytochemistry
    • Mouse neuroblastoma × rat glioma hybrid NG108-15 cells (Tanaka, T. et al. (2012) Biochim. Biophys. Acta 1820, 1035.).
    Indirect flow cytometry
    • Cell surface detection of nAChRα7 in live intact Jurkat (human T cell leukemia) cell line:
      Cell surface detection of nAChRα7 in live intact Jurkat (human T cell leukemia) cell line:
      ___ Cells + goat-anti-rabbit-Cy5.
      ___ Cells + Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody (#ANC-007), (1:25) + goat-anti-rabbit-Cy5.
    • The blocking peptide is not suitable for this application.
    Live cell imaging / Immunocytochemistry
    • Expression of nAChRα7 in rat PC12 cells
      Expression of nAChRα7 in rat PC12 cells
      Cell surface detection of nAChRα7 in live intact rat PC12 pheochromocytoma cells. A. Extracellular staining of cells with Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody (#ANC-007), (1:25), followed by goat anti-rabbit-AlexaFluor-594 secondary antibody (red). B. Live view of the cells. C. Merge of A and B.
    References
    1. Albuquerque, E.X. et al (2009) Physiol. Rev. 89, 73.
    2. Karlin, A. et al. (1986) Ann. N.Y. Acad. Sci. 463, 53.
    3. Kalamida, D. et al. (2007) FEBS J. 274, 3799.
    4. Fu, X.W. et al. (2009) Am. J. Respir. Mol. Biol. 41, 93.
    5. De Rosa, M.J. et al. (2009) Life Sci. 85, 449.
    6. Potter, D. et al. (2006) Schizophr. Bull. 32, 692.
    7. Haberberger, R.V. et al. (2004) Auton. Neurosci. 113, 32.
    Scientific background

    Acetylcholine, released by cholinergic neurons, activates two groups of acetylcholine receptors (AChRs); muscarinic AChRs (mAChRs) which belong to the superfamily of G-protein coupled receptors (GPCRs) and nicotinic AChRs (nAChRs) which belong to the ligand-gated ion channel superfamily. nAChRs also respond to nicotine, hence their name1. These channel receptors are usually non-selective cation channels activated upon ligand binding which ultimately leads to the depolarization of postsynaptic cell membranes.

    To date, 17 different but related subunits of nAChRs have been identified and cloned. They consist of a subunits (α1-10), which is responsible for the binding of ligands. In fact, this subunit includes a Cys-loop in the first extracellular domain that is required for agonist binding2. The other subunits responsible for making up the active receptor are the β (β1-4), γ, δ and ε subunits3. Structurally, all subunits have the following: a conserved large extracellular N-terminal domain, 3 conserved transmembrane domains, a variable cytoplasmic loop and a fourth transmembrane domain with a short extracellular C-terminal domain.  An active nAChR is generally a heteropentamer (homopentamers also exist) of these various subunits organized around a central pore1. However, the α7 subunit mainly forms homomeric functional structures, although functional channels have been observed with its association with α5, β2 or β3 subunits1.

    Interestingly, the α7 nAChR is the only subunit to be activated by two endogenous ligands: acetylcholine and choline1.

    All α subunits are expressed in neuronal cells except for the α1 subunit which is specifically expressed in skeletal muscle. They are also expressed in non-neuronal cells such as bronchial epithelial cells4, as well lymphocytes5. The diversity of these receptors and their functional organization gives rise to unique properties and functions. The α4β2 receptor composition makes up a high affinity nicotinic receptor. In fact, its upregulation (mainly expressed by the increase of functional receptors at the membrane and not expression per se) is responsible for the increased appearance of binding sites following nicotine administration1,3.

    α7 nAChR seems to be involved in the impairment of sensory gating in schizophrenic individuals. Indeed, many polyphormisms have been detected in the gene promoter of the receptor6. There is also an association of the receptor with nociception as it, along with α2 and α10 subunits are expressed in DRGs, the nociceptive center7.

    Application key:

    CBE- Cell-based ELISA, FC- Flow cytometry, ICC- Immunocytochemistry, IE- Indirect ELISA, IF- Immunofluorescence, IFC- Indirect flow cytometry, IHC- Immunohistochemistry, IP- Immunoprecipitation, LCI- Live cell imaging, N- Neutralization, WB- Western blot

    Species reactivity key:

    H- Human, M- Mouse, R- Rat
    Last update: 02/09/2020

    Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody (#ANC-007) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot, immunohistochemistry, immunocytochemistry, live cell imaging, and indirect flow cytometry applications. It has been designed to recognize nAChRα7 from mouse, rat, and human samples.

    For research purposes only, not for human use

    Applications

    Specifications

    Scientific Background

    Citations

    Citations
    KO validation citations
    1. Western blot analysis of human PDAC cells. Tested in siRNA-treated cells.
      Throm, V.M. et al.  (2018) Oncotarget9, 11734.
    2. Immunohistochemistry of mouse purified T-cells. Tested in NK1R-/- mice.
      Nishio, T. et al. (2017) J. Gastroenterol. 52, 965.
    Western blot citations
    1. Human PDAC cells. Tested in siRNA-treated cells.
      Throm, V.M. et al.  (2018) Oncotarget9, 11734.
    Immunohistochemistry citations
    1. Mouse purified T-cells. Tested in NK1R-/- mice.
      Nishio, T. et al. (2017) J. Gastroenterol. 52, 965.
    Immunocytochemistry citations
    1. Mouse neuroblastoma x rat glioma hybrid NG108-15 cells.
      Tanaka, T. et al. (2012) Biochim. Biophys. Acta 1820, 1035.
    Immunofluorescence citations
    1. Mouse purified T-cells. Tested in NK1R-/- mice.
      Nishio, T. et al. (2017) J. Gastroenterol. 52, 965.
    Indirect flow cytometry citations
    1. Human PANC-1 and COLO357 live, intact cells.
      Throm, V.M. et al.  (2018) Oncotarget9, 11734.
    More product citations
    1. Kiss, T. et al. (2014) PLoS ONE 9, e109538.
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